cysteine has been researched along with flavin-adenine dinucleotide in 85 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 18 (21.18) | 18.7374 |
1990's | 26 (30.59) | 18.2507 |
2000's | 25 (29.41) | 29.6817 |
2010's | 14 (16.47) | 24.3611 |
2020's | 2 (2.35) | 2.80 |
Authors | Studies |
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Ohnishi, T; Salerno, JC | 1 |
Kenney, WC; Singer, TP | 2 |
Prongay, AJ; Williams, CH | 2 |
Ahmed, SA; Claiborne, A; Schulz, GE; Stehle, T | 1 |
Claiborne, A; Poole, LB | 1 |
Kaminsky, LS; Lee, JJ | 1 |
Katsume, T; Muratsubaki, H | 1 |
Ikeda, Y; Okamura-Ikeda, K; Tanaka, K | 1 |
Funaba, T; Izaki, K; Tashiro, Y | 1 |
Cronin, JR; Edmondson, DE; Hendriks, R; Kenney, WC; Singer, TP; Walker, WH | 1 |
Juchau, MR; Krasner, J; Yaffe, SJ | 1 |
Ronchi, S; Williams, CH | 1 |
Hayashi, R; Hosomi, S; Mizoguchi, T; Uehara, K; Yonezawa, M | 1 |
Kearney, EB; Seng, R; Singer, TP; Walker, WH | 1 |
Brumby, PE; Casola, L; Massey, V | 1 |
Krauth-Siegel, RL; Schirmer, I; Schirmer, RH; Untucht-Grau, R | 1 |
Hopkins, N; Williams, CH | 2 |
Williams, CH | 1 |
Hidaka, M; Masaki, H; Niimura, Y; Nishino, T; Ohnishi, K; Suzuki, H; Uozumi, T | 1 |
Bui, BT; Florentin, D; Izumi, Y; Marquet, A; Ohshiro, T; Yamamoto, M | 1 |
Campbell, WH; Dwivedi, UN; Shiraishi, N | 1 |
Jorns, MS; Raibekas, AA | 2 |
Bichler, V; Brandsch, R; Decker, K; Mauch, L | 1 |
Krishna, TS; Kuriyan, J; Waksman, G; Williams, CH | 1 |
Claiborne, A; Schulz, GE; Stehle, T | 1 |
Cesura, AM; Da Prada, M; Gottowik, J; Lang, G; Malherbe, P | 1 |
Brandsch, R; Henninger, HP; Stoltz, M | 1 |
Barber, MJ; Quinn, GB; Smith, ET; Trimboli, AJ | 1 |
Claiborne, A; Hol, WG; Yeh, JI | 1 |
Hirashiki, I; Hiro, I; Ito, A; Ogata, F; Tsugeno, Y | 1 |
Gorren, AC; Mayer, B; Schmidt, K; Schrammel, A | 1 |
Mulrooney, SB; Williams, CH | 1 |
Rao, GR; Sengupta, S; Subbarap Shaila, M | 1 |
Mulrooney, SB; Veine, DM; Wang, PF; Williams, CH | 1 |
Hu, Z; Poulton, JE | 1 |
Amzel, LM; Bianchet, MA; Foster, CE; Talalay, P; Zhao, Q | 1 |
Poulsen, LL; Robertus, JD; Suh, JK; Ziegler, DM | 1 |
Chen, SG; Monnier, VM; Takahashi, M; Wu, X | 1 |
Büchert, T; Fritz, G; Huber, H; Kroneck, PM; Stetter, KO | 1 |
Chang, SI; Choi, JD; Chong, CK; Shin, HJ | 1 |
Banerjee, A; Dangott, LJ; Fitzpatrick, PF; Gadda, G | 1 |
Casey, PJ; Coates, RM; Digits, JA; Pyun, HJ; Tschantz, WR | 1 |
Gomes, CM; Lemos, RS; Teixeira, M | 1 |
Fujii, J; Fujii, T; Fujiwara, N; Taniguchi, N | 1 |
Fass, D; Gross, E; Kaiser, CA; Sevier, CS; Vala, A | 1 |
Bardwell, JC; Collet, JF | 1 |
Ito, A; Ma, J | 1 |
Dick, S; Frey, HE; Lepock, JR; Siemann, S; Viswanatha, T | 1 |
Hofhaus, G; Lee, JE; Lisowsky, T; Rosenberg, B; Tews, I | 1 |
Dailey, HA; Dailey, TA; Rose, JP; Wang, BC; Wu, CK | 1 |
Blaesse, M; Huber, R; Kupke, T; Steinbacher, S | 1 |
Munro, AW; Roitel, O; Scrutton, NS | 1 |
Kirchner, U; Müller, R; van Berkel, WJ; Westphal, AH | 1 |
NAIR, PM; VAIDYANATHAN, CS | 1 |
OSAJIMA, Y; YAMAFUJI, K | 1 |
LEINWEBER, FJ; MONTY, KJ | 1 |
Daff, S | 1 |
Green, J; Paget, MS | 1 |
Arcari, P; Masullo, L; Masullo, M; Ruggiero, A; Ruocco, MR | 1 |
Bruckner, RC; Hassan-Abdallah, A; Jorns, MS; Zhao, G | 1 |
Hassan-Abdallah, A; Jorns, MS; Zhao, G | 1 |
Drew, DP; Fincher, GB; Lahnstein, J; Lunde, C | 1 |
Kutchan, TM; Macheroux, P; Winkler, A | 1 |
Bates, JN; Hashmi-Hill, MP; Lewis, SJ; Robertson, TP; Sandock, K | 1 |
Inanaga, H; Ito, K; Numata, T; Nureki, O; Osawa, T; Tomita, K | 1 |
Chen, CL; Chen, YR; Garg, V; Green-Church, KB; Hu, K; Kang, PT; Zhang, L | 1 |
Ali, V; Husain, A; Jeelani, G; Nozaki, T; Sato, D; Soga, T; Suematsu, M | 1 |
Dobritzsch, D; Lindqvist, Y; Lohkamp, B; Voevodskaya, N | 1 |
Arai, S; Blaber, M; Kurihara, K; Kuroki, R; Morimoto, S; Shoyama, Y; Takeuchi, A; Tamada, T; Taura, F | 1 |
Binda, C; Boy-Röttger, S; Buroni, S; Chiarelli, LR; Cole, ST; De Rossi, E; Degiacomi, G; Dhar, N; Dyson, PJ; Edmondson, DE; Fullam, E; Lucarelli, AP; Mattevi, A; McKinney, JD; Molteni, E; Neres, J; Pasca, MR; Pojer, F; Read, RJ; Riccardi, G; Zanoni, G | 1 |
Hwang, S; Kim, S; Lazar, P; Lee, KO; Lee, KW; Lee, SY; Lee, Y; Moon, JC; Shon, Y; Thangapandian, S | 1 |
Fan, S; Hou, C; Lang, Q; Liu, A | 1 |
Ferri, S; Kojima, K; Shiota, M; Sode, K; Tsugawa, W; Yamazaki, T; Yoshimatsu, K | 1 |
Capacho, AS; Machuqueiro, M; Teixeira, VH | 1 |
Boyd, JM; Carabetta, VJ; Dubnau, D; Krebs, C; Martinie, RJ; Mashruwala, AA; Tanner, AW | 1 |
Tao, P; Zhou, H; Zoltowski, BD | 1 |
Barbiroli, A; Barile, M; Bonomi, F; Eberini, I; Galluccio, M; Gianazza, E; Iametti, S; Indiveri, C; Leone, P; Tolomeo, M; Vrenna, F | 1 |
Shao, W; Wen, B; Xu, L; Yao, P; Zhang, Y; Zheng, W; Zhou, Z; Zhu, G | 1 |
Bou-Nader, C; Dozova, N; Hamdane, D; Lacombat, F; Plaza, P | 1 |
Campbell, AC; LeBlanc, S; Nam, HG; Schuermann, JP; Sobrado, P; Sultana, N; Tanner, JJ; Valentino, H | 1 |
Gudim, I; Hammerstad, M; Hersleth, HP | 1 |
4 review(s) available for cysteine and flavin-adenine dinucleotide
Article | Year |
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Biochemistry of covalently bound flavins.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Amino Acids; Animals; Bacteria; Binding Sites; Chemical Phenomena; Chemistry; Cysteine; Cytochromes; Flavin-Adenine Dinucleotide; Flavins; Histidine; Indoles; Monoamine Oxidase; Mycotoxins; Oxidation-Reduction; Oxidoreductases; Oxidoreductases, N-Demethylating; Protein Binding; Pyrroles; Riboflavin; Succinate Dehydrogenase; Thiamine | 1974 |
Glutathione reductase from human erythrocytes: amino-acid sequence of the structurally known FAD-binding domain.
Topics: Amino Acid Sequence; Binding Sites; Cysteine; Dihydrolipoamide Dehydrogenase; Erythrocytes; Flavin-Adenine Dinucleotide; Glutathione Reductase; Humans; NADP; Phosphates; Protein Conformation; Trypsin | 1981 |
Mechanism and structure of thioredoxin reductase from Escherichia coli.
Topics: Catalysis; Cysteine; Dihydrolipoamide Dehydrogenase; Disulfides; Escherichia coli; Flavin-Adenine Dinucleotide; Flavoproteins; Glutathione Reductase; NADP; Oxidation-Reduction; Oxidoreductases; Protein Structure, Tertiary; Structure-Activity Relationship; Thioredoxin-Disulfide Reductase | 1995 |
Bacterial redox sensors.
Topics: Bacteria; Bacterial Proteins; Benzoquinones; Cysteine; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Hemeproteins; Iron-Sulfur Proteins; NAD; NADP; Oxidation-Reduction; Oxidative Stress; Signal Transduction | 2004 |
81 other study(ies) available for cysteine and flavin-adenine dinucleotide
Article | Year |
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Tetranuclear and binuclear iron-sulfur clusters in succinate dehydrogenase: a method of iron quantitation by formation of paramagnetic complexes.
Topics: Binding Sites; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Iron; Iron-Sulfur Proteins; Metalloproteins; Nitric Oxide; Protein Binding; Protein Conformation; Succinate Dehydrogenase; Sulfur | 1976 |
Evidence for a thioether linkage between the flavin and polypeptide chain of Chromatium cytochrome c 552.
Topics: Acetals; Chemical Phenomena; Chemistry; Chromatium; Cysteine; Cytochrome c Group; Dithionite; Flavin-Adenine Dinucleotide; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Spectrophotometry; Zinc | 1977 |
Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue.
Topics: Amino Acid Sequence; Anaerobiosis; Binding Sites; Cysteine; Dithionite; Escherichia coli; Flavin-Adenine Dinucleotide; Mathematics; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Potentiometry; Recombinant Proteins; Spectrophotometry; Thioredoxin-Disulfide Reductase | 1992 |
The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution.
Topics: Crystallization; Cysteine; Enterococcus faecalis; Flavin-Adenine Dinucleotide; Models, Molecular; Peroxidases; Protein Conformation; X-Ray Diffraction | 1990 |
Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs.
Topics: Binding Sites; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Protein Binding; Spectrophotometry; Thioredoxin-Disulfide Reductase | 1990 |
The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid.
Topics: Amino Acid Sequence; Cysteine; Dithiothreitol; Enterococcus faecalis; Flavin-Adenine Dinucleotide; Hydrogen Peroxide; Isoelectric Focusing; Kinetics; Molecular Sequence Data; NAD; Neurotransmitter Agents; Nitrobenzoates; Oxidation-Reduction; Peptide Fragments; Peroxidases; Protein Denaturation; Spectrophotometry; Sulfhydryl Compounds; Trypsin | 1989 |
Fluorescence probing of the function-specific cysteines of rat microsomal NADPH-cytochrome P-450 reductase.
Topics: Adenine Nucleotides; Animals; Chromatography, High Pressure Liquid; Cysteine; Cytochrome c Group; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Fluorescence; Male; Microsomes, Liver; NADPH-Ferrihemoprotein Reductase; Rats; Rats, Inbred Strains; Structure-Activity Relationship; Trypsin | 1986 |
Characterization of fumarate reductase from baker's yeast: essential sulfhydryl group for binding of FAD.
Topics: Apoenzymes; Cysteine; Dithionitrobenzoic Acid; Flavin-Adenine Dinucleotide; Kinetics; Saccharomyces cerevisiae; Succinate Dehydrogenase | 1985 |
An essential cysteine residue located in the vicinity of the FAD-binding site in short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria.
Topics: Acyl-CoA Dehydrogenase, Long-Chain; Amino Acids; Animals; Binding Sites; Chloromercuribenzoates; Cysteine; Ethylmaleimide; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Kinetics; Methylmercury Compounds; Mitochondria, Liver; p-Chloromercuribenzoic Acid; Rats; Spectrophotometry | 1985 |
Mechanism of mercuric chloride resistance in microorganisms. 3. Purification and properties of a mercuric ion reducing enzyme from Escherichia coli bearing R factor.
Topics: Ammonium Sulfate; Apoproteins; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Thin Layer; Cysteine; D-Amino-Acid Oxidase; Dithiothreitol; Drug Resistance, Microbial; Escherichia coli; Extrachromosomal Inheritance; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glutathione; Mercaptoethanol; Mercury; NADP; Spectrophotometry | 1974 |
The covalently bound flavin of Chromatium cytochrome c552. 1. Evidence for cysteine thiohemiacetal at the 8 alpha position.
Topics: Acetals; Binding Sites; Chromatium; Cysteine; Cytochromes; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Flavins; Molecular Conformation; Protein Binding; Sulfhydryl Compounds | 1974 |
Model systems for aromatic nitro group reduction--relationships to tissue catalyzed reagents.
Topics: Aminobenzoates; Animals; Benzoates; Biological Transport, Active; Blood; Carbon Monoxide; Cysteine; Dialysis; Electrons; Female; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glutathione; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Indicators and Reagents; Liver; Male; Mice; Models, Biological; NAD; NADP; Oxidation-Reduction; Placenta; Pregnancy; Rats; Tissue Extracts | 1970 |
The isolation and primary structure of a peptide containing the oxidation-reduction active cystine of Escherichia coli thioredoxin reductase.
Topics: Amino Acid Sequence; Amino Acids; Bacterial Proteins; Binding Sites; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Cystine; Disulfides; Electron Transport; Escherichia coli; Flavin-Adenine Dinucleotide; Maleimides; Molecular Weight; NADP; Oxidation-Reduction; Oxidoreductases; Pepsin A; Peptides; Sulfhydryl Compounds; Thiocyanates | 1972 |
Effect of adenine on the riboflavin-sensitized photoreaction. I. Effect of adenine on the photodynamic inactivation of yeast alcohol dehydrogenase in the presence of riboflavin.
Topics: Adenine; Alcohol Oxidoreductases; Cysteine; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Fluoresceins; Methylene Blue; Photochemistry; Riboflavin; Saccharomyces | 1971 |
Sequence and structure of a cysteinyl flavin peptide from monoamine oxidase.
Topics: Amino Acid Sequence; Aminopeptidases; Binding Sites; Chromatography, Paper; Cysteine; Electrophoresis, Paper; Flavin-Adenine Dinucleotide; Fluorometry; Formates; Glycine; Hydrolysis; Indicators and Reagents; Liver; Monoamine Oxidase; Oxidation-Reduction; Peptides; Protein Binding; Serine; Spectrophotometry; Tyrosine | 1971 |
The reversible conversion of lipoyl dehydrogenase to an artifactual enzyme by oxidation of sulfhydryl groups.
Topics: Catalysis; Chemical Phenomena; Chemistry; Copper; Cysteine; Dihydrolipoamide Dehydrogenase; Flavin-Adenine Dinucleotide; Fluorescence; Sulfhydryl Compounds | 1966 |
Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S.
Topics: Cysteine; Dihydrolipoamide Dehydrogenase; Disulfides; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Serine; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Compounds | 1995 |
Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides.
Topics: Binding Sites; Coloring Agents; Cysteine; Dihydrolipoamide Dehydrogenase; Disulfides; Electron Transport; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; NAD; NADP; Oxidation-Reduction; Phenazines; Serine; Viologens | 1995 |
Role of cysteine 337 and cysteine 340 in flavoprotein that functions as NADH oxidase from Amphibacillus xylanus studied by site-directed mutagenesis.
Topics: Amino Acid Sequence; Base Sequence; Cysteine; Enzyme Stability; Flavin-Adenine Dinucleotide; Flavoproteins; Gram-Negative Facultatively Anaerobic Rods; Kinetics; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; NADH, NADPH Oxidoreductases; Oligodeoxyribonucleotides; Plasmids; Recombinant Proteins; Restriction Mapping; Spectrophotometry | 1995 |
Stimulatory factors for enzymatic biotin synthesis from dethiobiotin in cell-free extracts of Escherichia coli.
Topics: Bacillus; Biotin; Cell Extracts; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Immunosuppressive Agents; NAD; NADP; S-Adenosylmethionine | 1995 |
Generation of multiple mutations in the same sequence via the polymerase chain reaction using a single selection primer.
Topics: Base Sequence; Binding Sites; Cysteine; DNA Primers; Escherichia coli; Flavin-Adenine Dinucleotide; Genetic Vectors; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Plasmids; Polymerase Chain Reaction; Recombinant Proteins | 1994 |
Affinity probing of flavin binding sites. 1. Covalent attachment of 8-(methylsulfonyl)FAD to pig heart lipoamide dehydrogenase.
Topics: Amino Acid Sequence; Animals; Azotobacter vinelandii; Binding Sites; Chromatography, High Pressure Liquid; Cysteine; Dihydrolipoamide Dehydrogenase; Flavin-Adenine Dinucleotide; Molecular Sequence Data; Myocardium; Protein Binding; Spectrophotometry; Swine | 1994 |
Affinity probing of flavin binding sites. 2. Identification of a reactive cysteine in the flavin domain of Escherichia coli DNA photolyase.
Topics: Amino Acid Sequence; Binding Sites; Catalysis; Cysteine; Deoxyribodipyrimidine Photo-Lyase; Escherichia coli; Flavin-Adenine Dinucleotide; Molecular Sequence Data; Pyrimidine Dimers; Tetrahydrofolates | 1994 |
Cysteine to serine replacements in 6-hydroxy-D-nicotine oxidase. Consequences for enzyme activity, cofactor incorporation, and formation of high molecular weight protein complexes with molecular chaperones (GroEL).
Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Chaperonin 60; Chromatography, Gel; Cysteine; DNA Mutational Analysis; Escherichia coli; Flavin-Adenine Dinucleotide; Gene Expression; Heat-Shock Proteins; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Oxidoreductases; Plasmids; Polymerase Chain Reaction; Recombinant Proteins; Serine | 1993 |
Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis.
Topics: Amino Acid Sequence; Binding Sites; Computer Graphics; Crystallography, X-Ray; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Models, Molecular; Models, Structural; Molecular Sequence Data; NADP; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Thioredoxin-Disulfide Reductase | 1994 |
NADH binding site and catalysis of NADH peroxidase.
Topics: Binding Sites; Catalysis; Crystallography; Cysteine; Enterococcus faecalis; Flavin-Adenine Dinucleotide; Hydrogen Peroxide; Models, Molecular; NAD; Peroxidases; Protein Structure, Tertiary; X-Ray Diffraction | 1993 |
Characterisation of wild-type and mutant forms of human monoamine oxidase A and B expressed in a mammalian cell line.
Topics: Cells, Cultured; Cysteine; Flavin-Adenine Dinucleotide; Humans; Isoenzymes; Kinetics; Monoamine Oxidase; Mutagenesis, Site-Directed; Recombinant Fusion Proteins; Transfection | 1993 |
The design of an alternative, covalently flavinylated 6-hydroxy-D-nicotine oxidase by replacing the FAD-binding histidine by cysteine and reconstitution of the holoenzyme with 8-(methylsulfonyl)FAD.
Topics: Coenzymes; Cysteine; Drug Design; Flavin-Adenine Dinucleotide; Flavins; Histidine; Kinetics; Oxidoreductases; Point Mutation; Structure-Activity Relationship | 1996 |
Thiol modification and site directed mutagenesis of the flavin domain of spinach NADH:nitrate reductase.
Topics: Amino Acid Sequence; Base Sequence; Circular Dichroism; Cysteine; Enzyme Inhibitors; Ethylmaleimide; Ferricyanides; Flavin-Adenine Dinucleotide; Flavins; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Nitrate Reductase (NADH); Nitrate Reductases; Oxidation-Reduction; Spectrophotometry; Spinacia oleracea; Structure-Activity Relationship; Sulfhydryl Reagents | 1996 |
Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution.
Topics: Amino Acid Sequence; Binding Sites; Cloning, Molecular; Crystallography, X-Ray; Cysteine; Enterococcus faecalis; Escherichia coli; Flavin-Adenine Dinucleotide; Macromolecular Substances; Models, Molecular; Oxidation-Reduction; Peroxidases; Protein Structure, Secondary; Recombinant Proteins; Sulfenic Acids | 1996 |
Characterization of rat monoamine oxidase A with noncovalently-bound FAD expressed in yeast cells.
Topics: Alanine; Animals; Cysteine; DNA, Complementary; Flavin-Adenine Dinucleotide; Kinetics; Kynuramine; Liver; Monoamine Oxidase; Monoamine Oxidase Inhibitors; Mutagenesis, Site-Directed; Pargyline; Protein Binding; Rats; Saccharomyces cerevisiae; Serotonin; Substrate Specificity | 1996 |
Thiols and neuronal nitric oxide synthase: complex formation, competitive inhibition, and enzyme stabilization.
Topics: Animals; Arginine; Biopterins; Calmodulin; Cysteine; Dithiothreitol; Enzyme Inhibitors; Enzyme Stability; Flavin-Adenine Dinucleotide; Heme; Mercaptoethanol; NADP; Neurons; Nitric Oxide Synthase; Protein Binding; Rats; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Compounds; Temperature | 1997 |
Evidence for two conformational states of thioredoxin reductase from Escherichia coli: use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation.
Topics: Adenine Nucleotides; Amino Acid Sequence; Binding Sites; Cysteine; Disulfides; Endopeptidases; Escherichia coli; Flavin-Adenine Dinucleotide; Fluorescent Dyes; Kinetics; Mutation; NADP; Peptide Fragments; Protein Conformation; Spectrometry, Fluorescence; Tetradecanoylphorbol Acetate; Thioredoxin-Disulfide Reductase | 1997 |
In vitro and in vivo regulation of assimilatory nitrite reductase from Candida utilis.
Topics: Ammonium Chloride; Candida; Chloromercuribenzoates; Cysteine; Enzyme Induction; Enzyme Repression; Flavin-Adenine Dinucleotide; Gene Expression Regulation, Enzymologic; Kinetics; NAD; NADP; Nitrite Reductase (NAD(P)H); Nitrite Reductases; p-Chloromercuribenzoic Acid | 1997 |
Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin.
Topics: Cysteine; Disulfides; Dithionite; Dithionitrobenzoic Acid; Dithiothreitol; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; NADP; Osmolar Concentration; Oxidation-Reduction; Protein Conformation; Protein Engineering; Spectrometry, Fluorescence; Structure-Activity Relationship; Sulfhydryl Compounds; Thioredoxin-Disulfide Reductase; Thioredoxins | 1998 |
Molecular analysis of (R)-(+)-mandelonitrile lyase microheterogeneity in black cherry.
Topics: Aldehyde-Lyases; Amino Acid Sequence; Base Sequence; Catalytic Domain; Cysteine; DNA Primers; DNA, Complementary; Flavin-Adenine Dinucleotide; Fruit; Gene Expression; Genes, Plant; Glycosylation; Isoenzymes; Molecular Sequence Data; Multigene Family; Protein Sorting Signals; Sequence Homology, Amino Acid | 1999 |
Crystal structure of human quinone reductase type 2, a metalloflavoprotein.
Topics: Animals; Binding Sites; Copper; Crystallization; Crystallography, X-Ray; Cysteine; Flavin-Adenine Dinucleotide; Flavoproteins; Histidine; Humans; Metalloproteins; Mice; NAD(P)H Dehydrogenase (Quinone); Rats; Solutions; Vitamin K | 1999 |
Lysine 219 participates in NADPH specificity in a flavin-containing monooxygenase from Saccharomyces cerevisiae.
Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADP; Oxidation-Reduction; Oxygenases; Phosphates; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Alignment; Substrate Specificity | 1999 |
Cloning of amadoriase I isoenzyme from Aspergillus sp.: evidence of FAD covalently linked to Cys342.
Topics: Amino Acid Oxidoreductases; Amino Acid Sequence; Aspergillus fumigatus; Base Sequence; Binding Sites; Cloning, Molecular; Cysteine; Enzyme Activation; Flavin-Adenine Dinucleotide; Flavins; Isoenzymes; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2000 |
Adenylylsulfate reductases from archaea and bacteria are 1:1 alphabeta-heterodimeric iron-sulfur flavoenzymes--high similarity of molecular properties emphasizes their central role in sulfur metabolism.
Topics: Adenosine Monophosphate; Amino Acid Motifs; Archaeoglobus fulgidus; Binding Sites; Cysteine; Desulfovibrio; Desulfovibrio vulgaris; Dimerization; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Genes, Bacterial; Iron; Iron-Sulfur Proteins; Models, Molecular; Molecular Weight; Operon; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Sequence Homology, Amino Acid; Spectrophotometry; Sulfur; Sulfur Compounds | 2000 |
Structural and functional role of cysteinyl residues in tobacco acetolactate synthase.
Topics: Acetolactate Synthase; Cysteine; Disulfides; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Herbicides; Kinetics; Mutagenesis, Site-Directed; Nicotiana; Peptide Fragments; Plants, Toxic; Protein Binding; Protein Conformation; Spectrophotometry; Thiocyanates | 2000 |
Identification of a cysteine residue in the active site of nitroalkane oxidase by modification with N-ethylmaleimide.
Topics: Amino Acid Sequence; Binding Sites; Chromatography, High Pressure Liquid; Cysteine; Dioxygenases; Ethylmaleimide; Flavin-Adenine Dinucleotide; Flavoproteins; Fusarium; Half-Life; Kinetics; Mass Spectrometry; Molecular Sequence Data; Oxygenases; Peptide Fragments; Peptide Mapping; Sequence Analysis, Protein; Trypsin; Valerates | 2000 |
Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.
Topics: Carbon-Sulfur Lyases; Cysteine; Farnesol; Flavin-Adenine Dinucleotide; Hydrogen Peroxide; Lysosomes; Models, Chemical; Sulfides | 2001 |
Acidianus ambivalens Complex II typifies a novel family of succinate dehydrogenases.
Topics: Amino Acid Sequence; Benzoquinones; Cell Membrane; Cysteine; Electron Spin Resonance Spectroscopy; Electron Transport Complex II; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; Iron; Models, Biological; Molecular Sequence Data; Multienzyme Complexes; Oxidation-Reduction; Oxidoreductases; Oxygen; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Succinate Dehydrogenase; Sulfhydryl Compounds; Sulfolobaceae; Sulfur; Ultraviolet Rays | 2001 |
Roles of N-terminal active cysteines and C-terminal cysteine-selenocysteine in the catalytic mechanism of mammalian thioredoxin reductase.
Topics: Animals; Baculoviridae; Catalysis; COS Cells; Cysteine; Electron Transport; Flavin-Adenine Dinucleotide; Insecta; Mammals; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Tertiary; Rats; Selenocysteine; Thioredoxin-Disulfide Reductase; Thioredoxins | 2001 |
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
Topics: Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Circular Dichroism; Crystallography, X-Ray; Cysteine; Dimerization; Disulfides; Electron Transport; Flavin-Adenine Dinucleotide; Fungal Proteins; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutation; Oxidoreductases; Oxygen; Pliability; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Subunits; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Structure-Activity Relationship | 2002 |
Disulfides out of thin air.
Topics: Amino Acid Motifs; Bacterial Proteins; Binding Sites; Catalysis; Conserved Sequence; Crystallography, X-Ray; Cysteine; Disulfides; Flavin-Adenine Dinucleotide; Fungal Proteins; Membrane Proteins; Models, Chemical; Oxidoreductases; Oxygen; Protein Disulfide-Isomerases; Protein Structure, Secondary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship; Water | 2002 |
Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable and active conformation of rat monoamine oxidase A.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cysteine; Enzyme Stability; Flavin-Adenine Dinucleotide; Humans; Kinetics; Molecular Sequence Data; Monoamine Oxidase; Point Mutation; Protein Conformation; Rats; Substrate Specificity; Tyrosine; Yeasts | 2002 |
Recombinant lysine:N(6)-hydroxylase: effect of cysteine-->alanine replacements on structural integrity and catalytic competence.
Topics: Alanine; Calorimetry, Differential Scanning; Cysteine; Dithionitrobenzoic Acid; Enzyme Stability; Flavin-Adenine Dinucleotide; Hot Temperature; Iopanoic Acid; Kinetics; Mixed Function Oxygenases; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Recombinant Proteins | 2002 |
The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre.
Topics: Binding Sites; Color; Conserved Sequence; Cysteine; Dimerization; Enzyme Activation; Flavin-Adenine Dinucleotide; Genetic Complementation Test; Mitochondrial Proteins; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Serine; Spectrophotometry; Structure-Activity Relationship | 2003 |
The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase.
Topics: Amino Acid Sequence; Animals; Crystallography, X-Ray; Cysteine; Dithiothreitol; Flavin-Adenine Dinucleotide; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Protein Structure, Quaternary; Proteins; Rats; Sequence Alignment | 2003 |
Structure of MrsD, an FAD-binding protein of the HFCD family.
Topics: Bacterial Proteins; Bacteriocins; Binding Sites; Carboxy-Lyases; Catalysis; Crystallography, X-Ray; Cysteine; Electrons; Escherichia coli; Flavin-Adenine Dinucleotide; Flavins; Flavoproteins; Models, Chemical; Models, Molecular; Oxygen; Peptides; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary | 2003 |
Electron transfer in flavocytochrome P450 BM3: kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Bacterial Proteins; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Flavins; Humans; Kinetics; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; NADPH-Ferrihemoprotein Reductase; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry | 2003 |
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD.
Topics: Amino Acid Sequence; Archaeoglobus fulgidus; Bacillus; Catalysis; Catechols; Chromatography, High Pressure Liquid; Cysteine; Dimerization; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Mixed Function Oxygenases; Models, Chemical; Models, Molecular; Molecular Sequence Data; NAD; Phenol; Plasmids; Protein Binding; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry; Temperature | 2003 |
AN INDOLE OXIDASE ISOLATED FROM THE LEAVES OF TECOMA STANS.
Topics: Aldehydes; Bignoniaceae; Chloromercuribenzoates; Chromatography; Copper; Cyanides; Cysteine; Dimercaprol; Dioxygenases; Electron Transport Complex IV; Flavin-Adenine Dinucleotide; Glutathione; Indoles; Ions; Metabolism; Oxazoles; Oximes; Phenanthrolines; Plants; Quinacrine; Quinolines; Research; Sulfhydryl Compounds | 1964 |
REDUCTION OF NITRATE TO AMMONIA BY ENZYMES ISOLATED FROM GREEN ALGAE.
Topics: Ammonia; Chlorophyta; Colorimetry; Cysteine; Dialysis; Eukaryota; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Freeze Drying; Hydrogen-Ion Concentration; Hydroxylamines; Nitrates; Nitrites; Oxidoreductases; Renal Dialysis; Research; Spectrophotometry | 1964 |
CYSTEINE BIOSYNTHESIS IN NEUROSPORA CRASSA. I. THE METABOLISM OF SULFITE, SULFIDE, AND CYSTEINESULFINIC ACID.
Topics: Amino Acids; Cysteine; Flavin-Adenine Dinucleotide; Metabolism; Molecular Biology; Mutation; NADP; Neurospora; Neurospora crassa; Research; Sulfides; Sulfinic Acids; Sulfites | 1965 |
An appraisal of multiple NADPH binding-site models proposed for cytochrome P450 reductase, NO synthase, and related diflavin reductase systems.
Topics: Alanine; Bacillus megaterium; Binding Sites; Catalysis; Cysteine; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; NADP; NADPH-Ferrihemoprotein Reductase; Nitric Oxide Synthase; Oxidation-Reduction; Spectrophotometry; Substrate Specificity | 2004 |
A 35 kDa NAD(P)H oxidase previously isolated from the archaeon Sulfolobus solfataricus is instead a thioredoxin reductase.
Topics: Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Archaea; Base Sequence; Binding Sites; Cloning, Molecular; Consensus Sequence; Cysteine; Disulfides; Enzyme Stability; Flavin-Adenine Dinucleotide; Kinetics; Molecular Sequence Data; Molecular Weight; Mutation; NADH, NADPH Oxidoreductases; NADPH Oxidases; Sequence Homology, Amino Acid; Sulfolobus solfataricus; Temperature; Thioredoxin-Disulfide Reductase | 2004 |
Biosynthesis of covalently bound flavin: isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein.
Topics: Apoenzymes; Bacillus; Binding Sites; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Mutagenesis; Oxidoreductases, N-Demethylating; Recombinant Proteins; Sarcosine Oxidase; Spectrophotometry | 2005 |
Role of the covalent flavin linkage in monomeric sarcosine oxidase.
Topics: Apoproteins; Bacillus; Bacterial Proteins; Catalysis; Cysteine; Flavin-Adenine Dinucleotide; Mutation; Sarcosine Oxidase | 2006 |
Heterologous expression of cDNAs encoding monodehydroascorbate reductases from the moss, Physcomitrella patens and characterization of the expressed enzymes.
Topics: Amino Acid Sequence; Ascorbic Acid; Bryopsida; Catalysis; Cysteine; DNA, Complementary; Escherichia coli; Flavin-Adenine Dinucleotide; Gene Expression; Kinetics; Molecular Sequence Data; NADH, NADPH Oxidoreductases; Reactive Oxygen Species; Transformation, Bacterial | 2007 |
6-S-cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity.
Topics: Cysteine; Flavin-Adenine Dinucleotide; Kinetics; Mutagenesis, Site-Directed; Mutation, Missense; Oxidation-Reduction; Oxidoreductases, N-Demethylating; Plant Proteins; Spectrum Analysis | 2007 |
Flavin adenine dinucleotide may release preformed stores of nitrosyl factors from the vascular endothelium of conscious rats.
Topics: Acetylcholine; Animals; Aorta, Thoracic; Cysteine; Endothelium, Vascular; Flavin-Adenine Dinucleotide; Injections, Intravenous; Male; NG-Nitroarginine Methyl Ester; Nitric Oxide; Nitric Oxide Synthase; Nitroprusside; Radioligand Assay; Rats; Rats, Sprague-Dawley; Receptor, Muscarinic M3; S-Nitrosothiols; Vasodilation | 2007 |
Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon.
Topics: Amino Acid Sequence; Anticodon; Bacteria; Bacterial Proteins; Binding Sites; Catalytic Domain; Conserved Sequence; Cysteine; Flavin-Adenine Dinucleotide; Molecular Sequence Data; RNA, Transfer; Uridine | 2009 |
Peroxynitrite-mediated oxidative modifications of complex II: relevance in myocardial infarction.
Topics: Amino Acid Sequence; Animals; Cell Hypoxia; Cyclic N-Oxides; Cysteine; Disulfides; Electron Transport Complex II; Flavin-Adenine Dinucleotide; Humans; Molecular Sequence Data; Molecular Weight; Muscle Cells; Myocardial Infarction; Oxidation-Reduction; Peroxynitrous Acid; Protein Subunits; Rats; Rats, Sprague-Dawley; Tyrosine | 2010 |
Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica.
Topics: Amino Acid Sequence; Animals; Antiprotozoal Agents; Catalytic Domain; Cysteine; Entamoeba histolytica; Enzyme Activation; Flavin-Adenine Dinucleotide; Iron; Iron-Sulfur Proteins; Metronidazole; Molecular Sequence Data; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Protozoan Proteins; Substrate Specificity | 2010 |
Insights into the mechanism of dihydropyrimidine dehydrogenase from site-directed mutagenesis targeting the active site loop and redox cofactor coordination.
Topics: Amino Acid Substitution; Animals; Arginine; Catalytic Domain; Cysteine; Dihydrouracil Dehydrogenase (NADP); Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Flavins; Glutamine; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Pyrimidines; Serine; Spectrophotometry; Swine | 2010 |
Structure and function of ∆1-tetrahydrocannabinolic acid (THCA) synthase, the enzyme controlling the psychoactivity of Cannabis sativa.
Topics: Animals; Berberine; Cannabis; Carbon Dioxide; Crystallography, X-Ray; Cysteine; Flavin-Adenine Dinucleotide; Glutamic Acid; Histidine; Intramolecular Oxidoreductases; Mutation; Protein Structure, Tertiary; Psychotropic Drugs; Structure-Activity Relationship; Tyrosine | 2012 |
Structural basis for benzothiazinone-mediated killing of Mycobacterium tuberculosis.
Topics: Antitubercular Agents; Bacterial Proteins; Crystallography, X-Ray; Cysteine; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Flavoproteins; Fluorescent Dyes; Kinetics; Lysine; Microbial Sensitivity Tests; Microbial Viability; Models, Molecular; Mutagenesis, Site-Directed; Mycobacterium smegmatis; Mycobacterium tuberculosis; Oxidation-Reduction; Oxidoreductases; Protein Structure, Tertiary; Protein Transport; Subcellular Fractions; Thiazines | 2012 |
Comparative molecular modeling study of Arabidopsis NADPH-dependent thioredoxin reductase and its hybrid protein.
Topics: Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Catalytic Domain; Cysteine; Electron Transport; Electrons; Flavin-Adenine Dinucleotide; Isoenzymes; Molecular Chaperones; Molecular Dynamics Simulation; Molecular Sequence Data; NADP; Protein Structure, Tertiary; Recombinant Fusion Proteins; Structure-Activity Relationship; Thioredoxin-Disulfide Reductase | 2012 |
Biofuel cell based self-powered sensing platform for L-cysteine detection.
Topics: Aspergillus; Benzothiazoles; Bioelectric Energy Sources; Copper; Cysteine; Electron Transport; Enzyme Activation; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Glucose; Glucose 1-Dehydrogenase; Oxygen; Sulfonic Acids; Vitamin K 3 | 2015 |
An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes.
Topics: Amino Acid Sequence; Catalytic Domain; Conserved Sequence; Cysteine; Flavin-Adenine Dinucleotide; Glucose 1-Dehydrogenase; Iron; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Sulfur | 2016 |
The role of electrostatics in TrxR electron transfer mechanism: A computational approach.
Topics: Amino Acid Motifs; Coenzymes; Cysteine; Electron Transport; Electrons; Flavin-Adenine Dinucleotide; Humans; Hydrogen-Ion Concentration; Molecular Dynamics Simulation; Monte Carlo Method; Mutation; Oxidation-Reduction; Poisson Distribution; Protein Domains; Protein Structure, Secondary; Selenocysteine; Static Electricity; Thioredoxin Reductase 1; Water | 2016 |
The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]
Topics: Bacillus subtilis; Bacterial Proteins; Cysteine; Flavin-Adenine Dinucleotide; Iron-Sulfur Proteins; Oxidation-Reduction; Phosphorylation; Phylogeny; Spores, Bacterial; Transcription Factors | 2017 |
Revealing Hidden Conformational Space of LOV Protein VIVID Through Rigid Residue Scan Simulations.
Topics: Algorithms; Amino Acids; Circadian Clocks; Computational Biology; Crystallography, X-Ray; Cysteine; Darkness; Entropy; Flavin-Adenine Dinucleotide; Fungal Proteins; Light; Molecular Dynamics Simulation; Neurospora crassa; Protein Conformation | 2017 |
Bacterial Production, Characterization and Protein Modeling of a Novel Monofuctional Isoform of FAD Synthase in Humans: An Emergency Protein?
Topics: Catalytic Domain; Cloning, Molecular; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Gene Expression; Humans; Isoenzymes; Kinetics; Models, Molecular; Nucleotidyltransferases; Oxidation-Reduction; Protein Conformation, alpha-Helical | 2018 |
Impacts of Cys392, Asp393, and ATP on the FAD Binding, Photoreduction, and the Stability of the Radical State of Chlamydomonas reinhardtii Cryptochrome.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Aspartic Acid; Chlamydomonas reinhardtii; Cryptochromes; Cysteine; Flavin-Adenine Dinucleotide; Light; Oxidation-Reduction; Protein Binding; Protein Stability | 2019 |
Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO.
Topics: Adenine; Amino Acid Sequence; Bacillus subtilis; Binding Sites; Cysteine; Flavin-Adenine Dinucleotide; Flavins; Kinetics; Models, Molecular; Oxidation-Reduction; Photochemical Processes; Protein Binding; tRNA Methyltransferases; Tyrosine | 2019 |
Structure and function of a flavin-dependent S-monooxygenase from garlic (
Topics: Biopolymers; Cysteine; Disulfides; Flavin-Adenine Dinucleotide; Garlic; Hydrogen Peroxide; Hydroxylation; Kinetics; NADP; Oxidation-Reduction; Oxygenases; Protein Conformation; Structure-Activity Relationship; Substrate Specificity; Sulfinic Acids | 2020 |
The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA) Provide Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductase.
Topics: Bacillus cereus; Bacterial Proteins; Crystallography, X-Ray; Cysteine; Flavin-Adenine Dinucleotide; Glucosamine; NADP; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Protein Structure, Quaternary; Staphylococcus aureus | 2020 |